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Structure and function of the EA1 surface layer of Bacillus anthracis

Author

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  • Adrià Sogues

    (Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB
    Structural Biology Brussels, Vrije Universiteit Brussel, VUB)

  • Antonella Fioravanti

    (Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB
    Structural Biology Brussels, Vrije Universiteit Brussel, VUB)

  • Wim Jonckheere

    (Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB
    Structural Biology Brussels, Vrije Universiteit Brussel, VUB)

  • Els Pardon

    (Structural Biology Brussels, Vrije Universiteit Brussel, VUB
    VIB-VUB Center for Structural Biology, VIB)

  • Jan Steyaert

    (Structural Biology Brussels, Vrije Universiteit Brussel, VUB
    VIB-VUB Center for Structural Biology, VIB)

  • Han Remaut

    (Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB
    Structural Biology Brussels, Vrije Universiteit Brussel, VUB)

Abstract

The Gram-positive spore-forming bacterium Bacillus anthracis is the causative agent of anthrax, a deadly disease mostly affecting wildlife and livestock, as well as representing a bioterrorism threat. Its cell surface is covered by the mutually exclusive S-layers Sap and EA1, found in early and late growth phases, respectively. Here we report the nanobody-based structural characterization of EA1 and its native lattice contacts. The EA1 assembly domain consists of 6 immunoglobulin-like domains, where three calcium-binding sites structure interdomain contacts that allow monomers to adopt their assembly-competent conformation. Nanobody-induced depolymerization of EA1 S-layers results in surface defects, membrane blebbing and cell lysis under hypotonic conditions, indicating that S-layers provide additional mechanical stability to the cell wall. Taken together, we report a complete model of the EA1 S-layer and present a set of nanobodies that may have therapeutic potential against Bacillus anthracis.

Suggested Citation

  • Adrià Sogues & Antonella Fioravanti & Wim Jonckheere & Els Pardon & Jan Steyaert & Han Remaut, 2023. "Structure and function of the EA1 surface layer of Bacillus anthracis," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42826-x
    DOI: 10.1038/s41467-023-42826-x
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    References listed on IDEAS

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    1. Ekaterina Baranova & Rémi Fronzes & Abel Garcia-Pino & Nani Van Gerven & David Papapostolou & Gérard Péhau-Arnaudet & Els Pardon & Jan Steyaert & Stefan Howorka & Han Remaut, 2012. "SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly," Nature, Nature, vol. 487(7405), pages 119-122, July.
    2. Kathryn Tunyasuvunakool & Jonas Adler & Zachary Wu & Tim Green & Michal Zielinski & Augustin Žídek & Alex Bridgland & Andrew Cowie & Clemens Meyer & Agata Laydon & Sameer Velankar & Gerard J. Kleywegt, 2021. "Highly accurate protein structure prediction for the human proteome," Nature, Nature, vol. 596(7873), pages 590-596, August.
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    Cited by:

    1. Christoph Buhlheller & Theo Sagmeister & Christoph Grininger & Nina Gubensäk & Uwe B. Sleytr & Isabel Usón & Tea Pavkov-Keller, 2024. "SymProFold: Structural prediction of symmetrical biological assemblies," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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